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Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from

DOI: 10.1107/S2053230X15016076 DOI Help
PMID: 26457523 PMID Help

Authors: Edgar Morales-rios (MRC Laboratory of Molecular Biology) , Martin G. Montgomery (MRC Laboratory of Molecular Biology) , Andrew Leslie (MRC Laboratory of Molecular Biology) , José J. García-trejo (Universidad Nacional Autónoma de México) , John E. Walker (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 71 , PAGES 1309 - 1317

State: Published (Approved)
Published: October 2015

Open Access Open Access

Abstract: The structures of F-ATPases have predominantly been determined from mitochondrial enzymes, and those of the enzymes in eubacteria have been less studied. Paracoccus denitrificans is a member of the α-proteobacteria and is related to the extinct protomitochondrion that became engulfed by the ancestor of eukaryotic cells. The P. denitrificans F-ATPase is an example of a eubacterial F-ATPase that can carry out ATP synthesis only, whereas many others can catalyse both the synthesis and the hydrolysis of ATP. Inhibition of the ATP hydrolytic activity of the P. denitrificans F-ATPase involves the ζ inhibitor protein, an α-helical protein that binds to the catalytic F1 domain of the enzyme. This domain is a complex of three α-subunits and three β-subunits, and one copy of each of the γ-, δ- and ∊-subunits. Attempts to crystallize the F1–ζ inhibitor complex yielded crystals of a subcomplex of the catalytic domain containing the α- and β-subunits only. Its structure was determined to 2.3 Å resolution and consists of a heterodimer of one α-subunit and one β-subunit. It has no bound nucleotides, and it corresponds to the `open' or `empty' catalytic interface found in other F-ATPases. The main significance of this structure is that it aids in the determination of the structure of the intact membrane-bound F-ATPase, which has been crystallized.

Journal Keywords: ?-Proteobacteria; Paracoccus Denitrificans; F-Atpase; Structure; Catalytic ?? Dimer.

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

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